Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q05928 (BTC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probetacellulin

Cleaved into the following chain:

  1. Betacellulin
    Short name=BTC
Gene names
Name:Btc
Synonyms:Bcn
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length177 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Growth factor that binds to EGFR, ERBB4 and other EGF receptor family members. Potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. Ref.3

Subunit structure

Monomer. Interacts with EGFR and ERBB4.

Subcellular location

Betacellulin: Secretedextracellular space.

Probetacellulin: Cell membrane; Single-pass type I membrane protein.

Tissue specificity

Found in several mouse tissues including kidney, uterus and liver, as well as in beta tumor cell line and MCF-7 cells. It is not detected in the brain.

Sequence similarities

Contains 1 EGF-like domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Ref.1
Chain32 – 177146Probetacellulin
PRO_0000300686
Chain32 – 11180Betacellulin
PRO_0000007492
Propeptide112 – 17766Removed in mature form
PRO_0000007493

Regions

Topological domain32 – 11887Extracellular Potential
Transmembrane119 – 13921Helical; Potential
Topological domain140 – 17738Cytoplasmic Potential
Domain65 – 10541EGF-like
Compositional bias146 – 1538Arg/Lys-rich (basic)

Amino acid modifications

Glycosylation341N-linked (GlcNAc...) Potential
Glycosylation421N-linked (GlcNAc...) Potential
Glycosylation521N-linked (GlcNAc...) Potential
Disulfide bond69 ↔ 82 By similarity
Disulfide bond77 ↔ 93 By similarity
Disulfide bond95 ↔ 104 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q05928 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 066BB34F0E13F82B

FASTA17719,664
        10         20         30         40         50         60 
MDPTAPGSSV SSLPLLLVLA LGLAILHCVV ADGNTTRTPE TNGSLCGAPG ENCTGTTPRQ 

        70         80         90        100        110        120 
KVKTHFSRCP KQYKHYCIHG RCRFVVDEQT PSCICEKGYF GARCERVDLF YLQQDRGQIL 

       130        140        150        160        170 
VVCLIVVMVV FIILVIGVCT CCHPLRKHRK KKKEEKMETL DKDKTPISED IQETNIA 

« Hide

References

« Hide 'large scale' references
[1]"Betacellulin: a mitogen from pancreatic beta cell tumors."
Shing Y., Christofori G., Hanahan D., Ono Y., Sasada R., Igarashi K., Folkman J.
Science 259:1604-1607(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 32-54; 64-71 AND 75-111.
Tissue: Pancreas.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Skin.
[3]"Betacellulin-induced beta cell proliferation and regeneration is mediated by activation of ErbB-1 and ErbB-2 receptors."
Oh Y.S., Shin S., Lee Y.J., Kim E.H., Jun H.S.
PLoS ONE 6:E23894-E23894(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L08394 mRNA. Translation: AAA40511.1.
AK076272 mRNA. Translation: BAC36281.1.
IPIIPI00114721.
PIRA37408.
RefSeqNP_031594.1. NM_007568.5.
UniGeneMm.2024.

3D structure databases

ProteinModelPortalQ05928.
SMRQ05928. Positions 63-111.
ModBaseSearch...

Proteomic databases

PRIDEQ05928.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000121044; ENSMUSP00000112765; ENSMUSG00000082361.
GeneID12223.
KEGGmmu:12223.

Organism-specific databases

CTD685.
MGIMGI:99439. Btc.

Phylogenomic databases

eggNOGNOG121071.
HOGENOMHOG000237352.
HOVERGENHBG004905.
InParanoidQ05928.
KOK09783.
OMATQSKRKG.
OrthoDBEOG4WH8N4.

Gene expression databases

ArrayExpressQ05928.
BgeeQ05928.
GenevestigatorQ05928.
GermOnlineENSMUSG00000029391. Mus musculus.

Family and domain databases

InterProIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR015497. EGF_rcpt_ligand.
[Graphical view]
PANTHERPTHR10740. PTHR10740. 1 hit.
PfamPF00008. EGF. 1 hit.
[Graphical view]
SMARTSM00181. EGF. 1 hit.
[Graphical view]
PROSITEPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio280627.
PMAP-CutDBQ05928.
SOURCESearch...

Entry information

Entry nameBTC_MOUSE
AccessionPrimary (citable) accession number: Q05928
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 3, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families